ID A0A127VXB2_SPOPS Unreviewed; 870 AA.
AC A0A127VXB2;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Phosphoenolpyruvate synthase {ECO:0000313|EMBL:AMQ05927.1};
GN ORFNames=AZE41_08355 {ECO:0000313|EMBL:AMQ05927.1};
OS Sporosarcina psychrophila (Bacillus psychrophilus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1476 {ECO:0000313|EMBL:AMQ05927.1, ECO:0000313|Proteomes:UP000071057};
RN [1] {ECO:0000313|EMBL:AMQ05927.1, ECO:0000313|Proteomes:UP000071057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6497 {ECO:0000313|EMBL:AMQ05927.1,
RC ECO:0000313|Proteomes:UP000071057};
RA Yan W.;
RT "Complete genome sequence of the Sporosarcina psychrophila DSM6497, a
RT psychrophila Bacillus that can mediate the Ca2+ precipitation.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP014616; AMQ05927.1; -; Genomic_DNA.
DR RefSeq; WP_067207964.1; NZ_CP014616.1.
DR AlphaFoldDB; A0A127VXB2; -.
DR STRING; 1476.AZE41_08355; -.
DR KEGG; spsy:AZE41_08355; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000071057; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR PANTHER; PTHR43615; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43615:SF1; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Pyruvate {ECO:0000313|EMBL:AMQ05927.1}.
FT DOMAIN 18..315
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 794..865
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT COILED 48..75
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 870 AA; 97665 MW; 692F68E9E70EEAA8 CRC64;
MKPYVLELRE IDKMSQMVVG GKGMNLGECS RIEGTLVPEG FCVTTEAYKR VIGENEELQQ
LLDQLAVQKV DERKRISEIS RKIRELIEGI EIEKGIEQDI DRCLLTFGLE HAYAVRSSAT
AEDLPFASFA GQHDTYLNII GRDKVLRHIS KCWASLFTDR AVIYRIQNGF DHSQVFLSVI
IQRMIFPQAS GILFTADPLT SNRKLLSIDA SFGLGEALVS GLVSADCYKV QEDEIVDKMI
APKKLAIYGL KEGGTETQQI NPDLQKSQTL TDQQILQLAR KGRQIEAYFG CPQDIEWCLV
EDTFYIVQSR PITTLFPVPE ANDQENHVYV SVGHQQMMTD PMKPLGLAFY LLTTPAPMRK
AGGRLFVDIT HSLASPVSRE ILVDTLGQSD PLIKDALMTI IERDFIKLLP TGDKELSPSS
SNKSMSSAGF QTQFKNNPTI VSDLIKSSET SINELKQTIQ TKSGSDLFDF ILEDLQQLKK
ILFDPQSLGV IMTAMDASSW INEKMNMWLG EKNVADTLSQ SVPNNITSEM GLALLDVADV
IRPYPEVIHY LQHVKDDNFL EGIVTFEGGQ ESQDAIIAYL NKYGMRCAGE IDMTKTRWSE
KPTTLVPMIL SNIKELEPNS GKRKFEQGRQ AALKKEQELV DRLMQLPDGK RKAEETKRVI
SLIRNFIGYR EYPKYGMISR YFVYKQALLK EAEQLVQANV IHKKEDIYYL TFEELREVVR
TKKLDFEIIS KRKNDYKLYG KLTPPRVLTS DGEIIAGKYK RENLPAGAIV GLPVSSGVIE
GRARVILNME EAVLKEGDIL VTSFTDPGWT PLFVSIKGLV TEVGGLMTHG AVIAREYGLP
AVVGVENATK LIKDGQRIRV NGTEGYIEIL
//
